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A streptavidin variant with slower biotin dissociation and increased mechanostabilityThe origins of femtomolar protein-ligand binding: hydrogen-bond cooperativity and desolvation energetics in the biotin-(strept)avidin binding siteA structural snapshot of an intermediate on the streptavidin-biotin dissociation pathwaySer45 plays an important role in managing both the equilibrium and transition state energetics of the streptavidin-biotin systemImproved affinity of engineered streptavidin for the Strep-tag II peptide is due to a fixed open conformation of the lid-like loop at the binding siteLigand exchange between proteins. Exchange of biotin and biotin derivatives between avidin and streptavidinDimer-Tetramer Transition between Solution and Crystalline States of Streptavidin and Avidin MutantsHow the biotin–streptavidin interaction was made even stronger: investigation via crystallography and a chimaeric tetramerEvolved streptavidin mutants reveal key role of loop residue in high-affinity bindingStreptavidin and its biotin complex at atomic resolutionThe structure of the SBP-Tag-streptavidin complex reveals a novel helical scaffold bridging binding pockets on separate subunits.Structural consequences of cutting a binding loop: two circularly permuted variants of streptavidinStructural Adaptation of a Thermostable Biotin-binding Protein in a Psychrophilic EnvironmentDevelopment of a Tetrameric Streptavidin Mutein with Reversible Biotin Binding Capability: Engineering a Mobile Loop as an Exit Door for BiotinStructure-based design and synthesis of a bivalent iminobiotin analog showing strong affinity toward a low immunogenic streptavidin mutantStructure-based design of a streptavidin mutant specific for an artificial biotin analogueReduced antibody response to streptavidin through site-directed mutagenesisFunctional loop dynamics of the streptavidin-biotin complexInfluence of Coulombic repulsion on the dissociation pathways and energetics of multiprotein complexes in the gas phase.External cavity laser biosensor.Synthesis of a biotin derivative of iberiotoxin: binding interactions with streptavidin and the BK Ca2+-activated K+ channel expressed in a human cell line.Flagellar hook flexibility is essential for bundle formation in swimming Escherichia coli cells.Imaging and three-dimensional reconstruction of chemical groups inside a protein complex using atomic force microscopy.Combined laser tweezers and dielectric field cage for the analysis of receptor-ligand interactions on single cells.Streptavidin crystals as nanostructured supports and image-calibration references for cryo-EM data collection.Mechanically driven ATP synthesis by F1-ATPase.Engineering soluble monomeric streptavidin with reversible biotin binding capability.Fast complementation of split fluorescent protein triggered by DNA hybridizationStructure-guided design of an engineered streptavidin with reusability to purify streptavidin-binding peptide tagged proteins or biotinylated proteins.Structure and catalytic properties of an engineered heterodimer of enolase composed of one active and one inactive subunitProtein translocation by bacterial toxin channels: a comparison of diphtheria toxin and colicin IaA robust method for production of MHC tetramers with small molecule fluorophores.Detecting the native ligand orientation by interfacial rigidity: SiteInterlock.Thermodynamic and structural consequences of flexible loop deletion by circular permutation in the streptavidin-biotin systemSizing the protein translocation pathway of colicin Ia channels.Cooperative hydrogen bond interactions in the streptavidin-biotin systemThree-Dimensional Characterization of Mechanical Interactions between Endothelial Cells and Extracellular Matrix during Angiogenic Sprouting.The chemical origin of enhanced signals from tip-enhanced Raman detection of functionalized nanoparticlesThe origin of the cooperativity in the streptavidin-biotin system: A computational investigation through molecular dynamics simulations.Directed evolution of streptavidin variants using in vitro compartmentalization.
P2860
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P2860
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年学术文章
@wuu
1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
@yue
1997年學術文章
@zh
1997年學術文章
@zh-hant
name
Structural studies of the streptavidin binding loop.
@ast
Structural studies of the streptavidin binding loop.
@en
type
label
Structural studies of the streptavidin binding loop.
@ast
Structural studies of the streptavidin binding loop.
@en
prefLabel
Structural studies of the streptavidin binding loop.
@ast
Structural studies of the streptavidin binding loop.
@en
P2093
P2860
P356
P1433
P1476
Structural studies of the streptavidin binding loop.
@en
P2093
I Le Trong
P S Stayton
R E Stenkamp
P2860
P304
P356
10.1002/PRO.5560060604
P577
1997-06-01T00:00:00Z